ArticleJournal of the American Chemical Society2015
Evidence for Functionally Relevant Encounter Complexes in Nitrogenase Catalysis.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 39 citations in OpenAlex.
- Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification.Nature communications · 2025Article
- Conformational control over proton-coupled electron transfer in metalloenzymes.Nature reviews. Chemistry · 2024Review
- Structural insights into the iron nitrogenase complex.Nature structural & molecular biology · 2024Article
- Fe protein docking transduces conformational changes to MoFe nitrogenase active site in a nucleotide-dependent manner.Communications chemistry · 2023Article
- Structures of the nitrogenase complex prepared under catalytic turnover conditions.Science (New York, N.Y.) · 2022Article
- Statistical analysis of PRSC advances · 2022Article
- Mechanical coupling in the nitrogenase complex.PLoS computational biology · 2021Article
- Reduction of Substrates by Nitrogenases.Chemical reviews · 2020Review
- Electron Transfer in Nitrogenase.Chemical reviews · 2020Review
- Chimeric Interaction of Nitrogenase-Like Reductases with the MoFe Protein of Nitrogenase.Chembiochem : a European journal of chemical biology · 2020Article
- Control of electron transfer in nitrogenase.Current opinion in chemical biology · 2018Review
- Crystal structure of VnfH, the iron protein component of vanadium nitrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Energy Transduction in Nitrogenase.Accounts of chemical research · 2018Article
- Conformationally Gated Electron Transfer in Nitrogenase. Isolation, Purification, and Characterization of Nitrogenase From Gluconacetobacter diazotrophicus.Methods in enzymology · 2018Article
- Determination of nucleoside triphosphatase activities from measurement of true inorganic phosphate in the presence of labile phosphate compounds.Analytical biochemistry · 2017Article
- Nitrogenase-mimic iron-containing chalcogels for photochemical reduction of dinitrogen to ammonia.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- CowN sustains nitrogenase turnover in the presence of the inhibitor carbon monoxide.The Journal of biological chemistryArticle
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Nitrogenase is the only enzyme that can convert atmospheric dinitrogen (N2) into biologically usable ammonia (NH3). To achieve this multielectron redox process, the nitrogenase component proteins, MoFe-protein (MoFeP) and Fe-protein (FeP), repeatedly associate and dissociate in an ATP-dependent manner, where one electron is transferred from FeP to MoFeP per association. Here, we provide experimental evidence that encounter complexes between FeP and MoFeP play a functional role in nitrogenase catalysis. The encounter complexes are stabilized by electrostatic interactions involving a positively charged patch on the β-subunit of MoFeP. Three single mutations (βAsn399Glu, βLys400Glu, and βArg401Glu) in this patch were generated in Azotobacter vinelandii MoFeP. All of the resulting variants displayed decreases in specific catalytic activity, with the βK400E mutation showing the largest effect. As simulated by the Thorneley-Lowe kinetic scheme, this single mutation lowered the rate constant for FeP-MoFeP association 5-fold. We also found that the βK400E mutation did not affect the coupling of ATP hydrolysis with electron transfer (ET) between FeP and MoFeP. These data suggest a mechanism where FeP initially forms encounter complexes on the MoFeP β-subunit surface en route to the ATP-activated, ET-competent complex over the αβ-interface.
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